Protein conformations have been investigated by means of several types of calculations. These include: 1) calculation of approximate energies for regular secondary regions, based on electrostatic energies, 2) investigations of folding pathways by extensive Monte Carlo generation of peptide conformations, in which the native conformation is favored but atomic overlaps are not permitted, and 3) more detailed energy calculations on protein fragments. In the first case, it was determined that, similar to other secondary conformation prediction methods, only about 2/3 of the residues are favored in their native conformation, if only local and medium range interactions are included. The implication is that long range interactions modify conformations of significant numbers of residues. Definite folding pathways were obtained for pancreatic trypsin inhibitor from the random generation. The activated state for the folding is found to correspond to the formation of the two strand beta sheet. Subsequently, multiple folding pathways were obtained. In the third case above, hypervariable regions of myeloma immunoglobulins have been optimized within the constraints imposed by the remainder of the molecule.